Cargando…

Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA

Dinoroseobacter shibae living in the photic zone of marine ecosystems is frequently exposed to oxygen that forms highly reactive species. Here, we analysed the adaptation of D. shibae to different kinds of oxidative stress using a GeLC-MS/MS approach. D. shibae was grown in artificial seawater mediu...

Descripción completa

Detalles Bibliográficos
Autores principales: Beier, Nicole, Kucklick, Martin, Fuchs, Stephan, Mustafayeva, Ayten, Behringer, Maren, Härtig, Elisabeth, Jahn, Dieter, Engelmann, Susanne
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8007024/
https://www.ncbi.nlm.nih.gov/pubmed/33780465
http://dx.doi.org/10.1371/journal.pone.0248865
_version_ 1783672414938333184
author Beier, Nicole
Kucklick, Martin
Fuchs, Stephan
Mustafayeva, Ayten
Behringer, Maren
Härtig, Elisabeth
Jahn, Dieter
Engelmann, Susanne
author_facet Beier, Nicole
Kucklick, Martin
Fuchs, Stephan
Mustafayeva, Ayten
Behringer, Maren
Härtig, Elisabeth
Jahn, Dieter
Engelmann, Susanne
author_sort Beier, Nicole
collection PubMed
description Dinoroseobacter shibae living in the photic zone of marine ecosystems is frequently exposed to oxygen that forms highly reactive species. Here, we analysed the adaptation of D. shibae to different kinds of oxidative stress using a GeLC-MS/MS approach. D. shibae was grown in artificial seawater medium in the dark with succinate as sole carbon source and exposed to hydrogen peroxide, paraquat or diamide. We quantified 2580 D. shibae proteins. 75 proteins changed significantly in response to peroxide stress, while 220 and 207 proteins were differently regulated by superoxide stress and thiol stress. As expected, proteins like thioredoxin and peroxiredoxin were among these proteins. In addition, proteins involved in bacteriochlophyll biosynthesis were repressed under disulfide and superoxide stress but not under peroxide stress. In contrast, proteins associated with iron transport accumulated in response to peroxide and superoxide stress. Interestingly, the iron-responsive regulator RirA in D. shibae was downregulated by all stressors. A rirA deletion mutant showed an improved adaptation to peroxide stress suggesting that RirA dependent proteins are associated with oxidative stress resistance. Altogether, 139 proteins were upregulated in the mutant strain. Among them are proteins associated with protection and repair of DNA and proteins (e. g. ClpB, Hsp20, RecA, and a thioredoxin like protein). Strikingly, most of the proteins involved in iron metabolism such as iron binding proteins and transporters were not part of the upregulated proteins. In fact, rirA deficient cells were lacking a peroxide dependent induction of these proteins that may also contribute to a higher cell viability under these conditions.
format Online
Article
Text
id pubmed-8007024
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-80070242021-04-07 Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA Beier, Nicole Kucklick, Martin Fuchs, Stephan Mustafayeva, Ayten Behringer, Maren Härtig, Elisabeth Jahn, Dieter Engelmann, Susanne PLoS One Research Article Dinoroseobacter shibae living in the photic zone of marine ecosystems is frequently exposed to oxygen that forms highly reactive species. Here, we analysed the adaptation of D. shibae to different kinds of oxidative stress using a GeLC-MS/MS approach. D. shibae was grown in artificial seawater medium in the dark with succinate as sole carbon source and exposed to hydrogen peroxide, paraquat or diamide. We quantified 2580 D. shibae proteins. 75 proteins changed significantly in response to peroxide stress, while 220 and 207 proteins were differently regulated by superoxide stress and thiol stress. As expected, proteins like thioredoxin and peroxiredoxin were among these proteins. In addition, proteins involved in bacteriochlophyll biosynthesis were repressed under disulfide and superoxide stress but not under peroxide stress. In contrast, proteins associated with iron transport accumulated in response to peroxide and superoxide stress. Interestingly, the iron-responsive regulator RirA in D. shibae was downregulated by all stressors. A rirA deletion mutant showed an improved adaptation to peroxide stress suggesting that RirA dependent proteins are associated with oxidative stress resistance. Altogether, 139 proteins were upregulated in the mutant strain. Among them are proteins associated with protection and repair of DNA and proteins (e. g. ClpB, Hsp20, RecA, and a thioredoxin like protein). Strikingly, most of the proteins involved in iron metabolism such as iron binding proteins and transporters were not part of the upregulated proteins. In fact, rirA deficient cells were lacking a peroxide dependent induction of these proteins that may also contribute to a higher cell viability under these conditions. Public Library of Science 2021-03-29 /pmc/articles/PMC8007024/ /pubmed/33780465 http://dx.doi.org/10.1371/journal.pone.0248865 Text en © 2021 Beier et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Beier, Nicole
Kucklick, Martin
Fuchs, Stephan
Mustafayeva, Ayten
Behringer, Maren
Härtig, Elisabeth
Jahn, Dieter
Engelmann, Susanne
Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA
title Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA
title_full Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA
title_fullStr Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA
title_full_unstemmed Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA
title_short Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA
title_sort adaptation of dinoroseobacter shibae to oxidative stress and the specific role of rira
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8007024/
https://www.ncbi.nlm.nih.gov/pubmed/33780465
http://dx.doi.org/10.1371/journal.pone.0248865
work_keys_str_mv AT beiernicole adaptationofdinoroseobactershibaetooxidativestressandthespecificroleofrira
AT kucklickmartin adaptationofdinoroseobactershibaetooxidativestressandthespecificroleofrira
AT fuchsstephan adaptationofdinoroseobactershibaetooxidativestressandthespecificroleofrira
AT mustafayevaayten adaptationofdinoroseobactershibaetooxidativestressandthespecificroleofrira
AT behringermaren adaptationofdinoroseobactershibaetooxidativestressandthespecificroleofrira
AT hartigelisabeth adaptationofdinoroseobactershibaetooxidativestressandthespecificroleofrira
AT jahndieter adaptationofdinoroseobactershibaetooxidativestressandthespecificroleofrira
AT engelmannsusanne adaptationofdinoroseobactershibaetooxidativestressandthespecificroleofrira